Photochemical interconversion between the red-absorbing (Pr) and the far-red-absorbing (Pfr) forms of the photosensory protein phytochrome initiates signal transduction in bacteria and higher plants. The Pr-to-Pfr transition commences with a rapid Z-to-E photoisomerization at the C15 = C16 methine bridge of the bilin prosthetic group. Here, we use femtosecond stimulated Raman spectroscopy to probe the structural changes of the phycocyanobilin chromophore within phytochrome Cph1 on the ultrafast time scale. The enhanced intensity of the C15-H hydrogen out-of-plane (HOOP) mode, together with the appearance of red-shifted CAC stretch and N - H in-plane rocking modes within 500 fs, reveal that initial distortion of the C15 = C16 bond occurs in the electronically excited I* intermediate. From I*, 85% of the excited population relaxes back to Pr in 3 ps, whereas the rest goes on to the Lumi-R photoproduct consistent with the 15% photochemical quantum yield. The C15-H HOOP and skeletal modes evolve to a Lumi-R-like pattern after 3 ps, thereby indicating that the C15 = C16 Z-to-E isomerization occurs on the excited-state surface.
|Original language||English (US)|
|Number of pages||6|
|Journal||Proceedings of the National Academy of Sciences of the United States of America|
|State||Published - Feb 10 2009|
- Photosensory proteins
- Plant signal transduction
- Time-resolved vibrational spectroscopy